3ZZK
Structure of an engineered aspartate aminotransferase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
A | 0004838 | molecular_function | L-tyrosine-2-oxoglutarate transaminase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0033585 | biological_process | L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PMP A 1397 |
Chain | Residue |
A | TYR65 |
A | SER243 |
A | SER245 |
A | LYS246 |
A | ARG254 |
A | SO41400 |
A | HOH2044 |
A | HOH2286 |
A | GLY102 |
A | GLY103 |
A | THR104 |
A | TRP130 |
A | HIS178 |
A | ASN183 |
A | ASP211 |
A | ALA213 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1398 |
Chain | Residue |
A | ARG315 |
A | GLN316 |
A | GLN319 |
A | HOH2289 |
A | HOH2418 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1399 |
Chain | Residue |
A | ARG122 |
A | GLN170 |
A | ARG360 |
A | ALA394 |
A | HOH2189 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 1400 |
Chain | Residue |
A | ILE13 |
A | GLY34 |
A | TRP130 |
A | ASN183 |
A | ARG374 |
A | PMP1397 |
A | HOH2044 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1401 |
Chain | Residue |
A | GLN33 |
A | ASN64 |
A | HOH2034 |
A | HOH2095 |
A | HOH2096 |
A | HOH2419 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1402 |
Chain | Residue |
A | TYR55 |
A | ASN300 |
A | HOH2337 |
A | HOH2341 |
A | HOH2421 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1403 |
Chain | Residue |
A | SER129 |
A | TRP130 |
A | PRO131 |
A | ASN183 |
A | PRO184 |
A | VAL370 |
A | SER372 |
A | HOH2422 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1404 |
Chain | Residue |
A | LYS134 |
A | ASN138 |
A | GLU143 |
A | VAL144 |
A | GOL1406 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1405 |
Chain | Residue |
A | PRO72 |
A | ARG76 |
A | HOH2117 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1406 |
Chain | Residue |
A | ASN138 |
A | GLY141 |
A | GOL1404 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG |
Chain | Residue | Details |
A | SER243-GLY256 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | GLY34 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | TRP130 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | ASN183 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC |
Chain | Residue | Details |
A | ARG374 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA |
Chain | Residue | Details |
A | LYS246 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 777 |
Chain | Residue | Details |
A | TRP130 | steric role |
A | ASP211 | proton shuttle (general acid/base) |
A | LYS246 | proton shuttle (general acid/base) |